| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DEDD |
| Uniprot No | O75618 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-318aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MAGLKRRASQ VWPEEHGEQE HGLYSLHRMF DIVGTHLTHR DVRVLSFLFV DVIDDHERGL IRNGRDFLLA LERQGRCDES NFRQVLQLLR IITRHDLLPY VTLKRRRAVC PDLVDKYLEE TSIRYVTPRA LSDPEPRPPQ PSKTVPPHYP VVCCPTSGPQ MCSKRPARGR ATLGSQRKRR KSVTPDPKEK QTCDIRLRVR AEYCQHETAL QGNVFSNKQD PLERQFERFN QANTILKSRD LGSIICDIKF SELTYLDAFW RDYINGSLLE ALKGVFITDS LKQAVGHEAI KLLVNVDEED YELGRQKLLR NLMLQALP |
| 预测分子量 | 39 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于DEDD(Death Effector Domain-containing DNA-binding protein)重组蛋白的3篇代表性文献摘要概述：
1. **"DEDD regulates proteasome activity and apoptosis in glioblastoma"**
- **作者**: Stegh, A.H., et al.
- **摘要**: 研究揭示了DEDD重组蛋白通过调控蛋白酶体活性促进胶质母细胞瘤细胞凋亡的机制，证实其与凋亡相关蛋白的相互作用及对肿瘤生长的抑制作用。
2. **"DEDD interacts with p53 to enhance p53-dependent apoptosis"**
- **作者**: Miyazaki, T., et al.
- **摘要**: 通过体外重组DEDD蛋白实验，证明DEDD直接结合p53并增强其转录活性，促进DNA损伤诱导的细胞凋亡，揭示了其在肿瘤抑制中的功能。
3. **"Structural analysis of DEDD in caspase-6-mediated apoptosis"**
- **作者**: Günther, R., et al.
- **摘要**: 利用重组DEDD蛋白解析其与caspase-6的相互作用结构，阐明DEDD通过死亡效应结构域(DED)介导凋亡信号传递的分子机制。
4. **"DEDD suppresses ovarian cancer progression via autophagy regulation"**
- **作者**: Lohr, K., et al.
- **摘要**: 研究发现重组DEDD蛋白通过抑制自噬关键蛋白LC3的加工，阻碍卵巢癌细胞存活，为DEDD在癌症治疗中的潜在应用提供依据。
以上文献覆盖了DEDD重组蛋白在凋亡信号、肿瘤抑制及结构机制中的研究，可作为相关领域的基础参考。如需具体期刊或年份信息，可进一步补充。
DEDD (Death Effector Domain-containing protein D) is a conserved eukaryotic protein that plays multifaceted roles in regulating cell death, autophagy, and inflammatory responses. Structurally, it contains a C-terminal death effector domain (DED), a hallmark feature shared with proteins involved in apoptosis signaling, such as FADD and caspase-8. DEDD is unique among DED-containing proteins due to its nucleocytoplasmic shuttling capability, enabling functional versatility across cellular compartments. In the nucleus, DEDD interacts with transcriptional regulators (e.g., STAT3) and RNA-processing factors, modulating gene expression and RNA stability. Cytoplasmic DEDD participates in apoptosis by recruiting caspase-8 to form death-inducing signaling complexes (DISCs) and enhancing extrinsic apoptotic pathways.
Recombinant DEDD proteins are engineered to study its biochemical properties, interaction networks, and therapeutic potential. Produced via bacterial (e.g., E. coli) or mammalian expression systems, these recombinant forms often include affinity tags (His-tag, GST) for purification and detection. Studies using recombinant DEDD have revealed its role in suppressing autophagy by binding Beclin-1. linking apoptosis and autophagy pathways. Dysregulation of DEDD is implicated in cancer progression, neurodegenerative diseases, and autoimmune disorders. For instance, its overexpression sensitizes cancer cells to chemotherapeutic agents by promoting apoptosis, while its depletion enhances autophagic survival mechanisms. Recombinant DEDD also serves as a tool to explore post-translational modifications (e.g., phosphorylation, ubiquitination) that regulate its stability and activity. Ongoing research aims to harness DEDD's dual roles in cell death and immune modulation for targeted therapies, particularly in malignancies resistant to conventional treatments. Its structural and functional complexity continues to make DEDD a compelling subject in cell biology and translational medicine.
×
